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Yorodumi- PDB-1tch: STRUCTURE-ACTIVITY RELATIONSHIPS OF MU-CONOTOXIN GIIIA: STRUCTURE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tch | ||||||
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Title | STRUCTURE-ACTIVITY RELATIONSHIPS OF MU-CONOTOXIN GIIIA: STRUCTURE DETERMINATION OF ACTIVE AND INACTIVE SODIUM CHANNEL BLOCKER PEPTIDES BY NMR AND SIMULATED ANNEALING CALCULATIONS | ||||||
Components | MU-CONOTOXIN GIIIA | ||||||
Keywords | NEUROTOXIN | ||||||
Function / homology | Mu-Conotoxin / Conotoxin, mu-type / Mu-conotoxin family signature. / sodium channel inhibitor activity / toxin activity / extracellular region / Mu-conotoxin GIIIA Function and homology information | ||||||
Method | SOLUTION NMR | ||||||
Authors | Lancelin, J.-M. / Kohda, D. / Inagaki, F. | ||||||
Citation | Journal: Biochemistry / Year: 1992 Title: Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Authors: Wakamatsu, K. / Kohda, D. / Hatanaka, H. / Lancelin, J.M. / Ishida, Y. / Oya, M. / Nakamura, H. / Inagaki, F. / Sato, K. #1: Journal: Biochemistry / Year: 1991 Title: Tertiary Structure of Conotoxin Giiia in Aqueous Solution Authors: Lancelin, J.-M. / Kohda, D. / Tate, S.-I. / Yanagawa, Y. / Abe, T. / Satake, M. / Inagaki, F. #2: Journal: J.Biol.Chem. / Year: 1991 Title: Active Site of Mu-Conotoxin Giiia, a Peptide Blocker of Muscle Sodium Channels Authors: Sato, K. / Ishida, Y. / Wakamatsu, K. / Kato, R. / Honda, H. / Ohizumi, Y. / Nakamura, H. / Ohya, M. / Lancelin, J.-M. / Kohda, D. / Inagaki, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tch.cif.gz | 12.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tch.ent.gz | 10.1 KB | Display | PDB format |
PDBx/mmJSON format | 1tch.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tch_validation.pdf.gz | 345 KB | Display | wwPDB validaton report |
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Full document | 1tch_full_validation.pdf.gz | 345.7 KB | Display | |
Data in XML | 1tch_validation.xml.gz | 2.4 KB | Display | |
Data in CIF | 1tch_validation.cif.gz | 2.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tc/1tch ftp://data.pdbj.org/pub/pdb/validation_reports/tc/1tch | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: RESIDUE HYP 7 IS A CIS HYDROXYPROLINE. / 2: THE C-TERMINAL CARBOXYLATE IS AMIDATED. | |||||||||
NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2535.023 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P01523 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
NMR software | Name: X-PLOR / Version: 2.1 / Developer: BRUNGER / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 1 |